Toggle Main Menu Toggle Search

Open Access padlockePrints

Mechanism-based inactivation of coenzyme B12-dependent 2-methyleneglutarate mutase by (Z)-glutaconate and buta-1,3-diene-2,3- dicarboxylate

Lookup NU author(s): Antonius Pierik, Diana Suarez, Shang-Min Tu, Professor Bernard Golding

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.


Abstract

In the presence of holo 2-methyleneglutarate mutase, buta-1,3-diene-2,3- dicarboxylate and (Z)-glutaconate [(Z)-pent-2-ene-1,5-dicarboxylate], but not (E)-glutaconate, each induced homolysis of the Co-C bond of coenzyme B 12 to afford cob(II)alamin and the 5′-deoxyadenosyl radical. The latter probably added to the double bond in (Z)-glutaconate and one of the double bonds in buta-1,3-diene-2,3-dicarboxylate to afford a corresponding "radical adduct". The formation of new radicals and cob(II)alamin was diagnosed by UV/Visible and EPR spectroscopy. (Z)-Glutaconate rapidly inactivated the mutase with formation of aquocobalamin, which was possibly derived by electron transfer from cob(II)alamin to the radical adduct. In contrast, buta-1,3-diene-2,3-dicarboxylate was a much slower inactivator. In this case, the spectroscopic data revealed a relatively stable complex of the radical adduct with cob(II)alamin in the active site of the enzyme. © Wiley-VCH Verlag GmbH & Co. KGaA, 2006.


Publication metadata

Author(s): Buckel W, Pierik AJ, Plett S, Alhapel A, Suarez D, Tu S-M, Golding BT

Publication type: Article

Publication status: Published

Journal: European Journal of Inorganic Chemistry

Year: 2006

Issue: 18

Pages: 3622-3626

ISSN (print): 1434-1948

ISSN (electronic): 1099-0682

Publisher: Wiley - VCH Verlag GmbH & Co. KGaA

URL: http://dx.doi.org/10.1002/ejic.200600405

DOI: 10.1002/ejic.200600405


Altmetrics

Altmetrics provided by Altmetric


Actions

Find at Newcastle University icon    Link to this publication


Share